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Q5HPT0 (CDSA_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphatidate cytidylyltransferase

EC=2.7.7.41
Alternative name(s):
CDP-DAG synthase
CDP-DG synthase
CDP-diacylglycerol synthase
Short name=CDS
CDP-diglyceride pyrophosphorylase
CDP-diglyceride synthase
CTP:phosphatidate cytidylyltransferase
Gene names
Name:cdsA
Ordered Locus Names:SERP0828
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the CDS family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionNucleotidyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphatidate cytidylyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Phosphatidate cytidylyltransferase
PRO_0000090754

Regions

Transmembrane9 – 2921Helical; Potential
Transmembrane46 – 6621Helical; Potential
Transmembrane70 – 9021Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane130 – 15021Helical; Potential
Transmembrane172 – 19221Helical; Potential
Transmembrane196 – 21621Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q5HPT0 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: B52A542C097449B9

FASTA26029,179
        10         20         30         40         50         60 
MKVRTLTAII ALLIFLPILL KGGLILMLFA FLLALIALKE LLNMNMIKFL SIPGLISALA 

        70         80         90        100        110        120 
LIIIMLPQDA GEWVQVIQLK GLIAMSFIVL SYTVLSKNRF SFMDAAFCLM SVAYVGIGFM 

       130        140        150        160        170        180 
YFYETRSEGL RYILFAFLIV WLTDTGAYIF GRLMGKHKLW PVISPNKTIE GFFGGILCSI 

       190        200        210        220        230        240 
LVPLVMQMFV DLHMNIWLLL LVTIVLSMFG QLGDLVESGF KRHFGVKDSG RILPGHGGIL 

       250        260 
DRFDSFMFVL PLLNILLIQT 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54181.1.
RefSeqYP_188410.1. NC_002976.3.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HPT0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000043839; EBSTAP00000042382; EBSTAG00000043837.
GeneID3240986.
GenomeReviewsGene locus SERP0828 in contig CP000029_GR.
KEGGser:SERP0828.
PATRIC19612529. VBIStaEpi130894_0807.
TIGRSERP0828.

Phylogenomic databases

eggNOGCOG0575.
GeneTreeEBGT00050000025310.
HOGENOMHBG732679.
OMAWILLIPS.
ProtClustDBCLSK885236.

Enzyme and pathway databases

BioCycSEPI176279:SERP0828-MONOMER.

Family and domain databases

InterProIPR000374. PC_trans.
[Graphical view]
KOK00981.
PfamPF01148. CTP_transf_1. 1 hit.
[Graphical view]
PROSITEPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDSA_STAEQ
AccessionPrimary (citable) accession number: Q5HPT0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families